Abstract
AbstractThe dysbindin domain-containing protein 1 (DBNDD1) is a conserved protein among higher eukaryotes whose structure and function are poorly investigated so far. Here, we present the backbone and side chain nuclear magnetic resonance assignments for the human DBNDD1 protein. Our chemical-shift based secondary structure analysis reveals the human DBNDD1 as an intrinsically disordered protein.
Funder
H2020 European Research Council
Friedrich-Schiller-Universität Jena
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Cited by
1 articles.
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1. NMR of proteins and nucleic acids;Nuclear Magnetic Resonance;2023-11-29